ID M5AWZ5_CAMLA Unreviewed; 732 AA.
AC M5AWZ5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=HypF {ECO:0000313|EMBL:BAN13319.1};
OS Campylobacter lari.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=201 {ECO:0000313|EMBL:BAN13319.1};
RN [1] {ECO:0000313|EMBL:BAN13319.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CF89-12 {ECO:0000313|EMBL:BAN13319.1};
RA Nakajima T., Matsubara K., Hayashi K., Nakanishi S., Moore J.E.,
RA Millar B.C., Murayama T., Matsuda M.;
RT "Gnetic characterization of the methionine sulfoxide reductase A (msrA)
RT locus in Campylobacter lari.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl
CC phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE
CC protein] + diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:55636,
CC Rhea:RHEA-COMP:14247, Rhea:RHEA-COMP:14392, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:76913,
CC ChEBI:CHEBI:139126, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|ARBA:ARBA00001186};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000256|ARBA:ARBA00004711}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000256|ARBA:ARBA00008097, ECO:0000256|PIRNR:PIRNR006256}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB702689; BAN13319.1; -; Genomic_DNA.
DR AlphaFoldDB; M5AWZ5; -.
DR UniPathway; UPA00335; -.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.110.120; -; 1.
DR Gene3D; 3.30.420.360; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.90.870.50; -; 1.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR InterPro; IPR004421; Carbamoyltransferase_HypF.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR041440; HypF_C.
DR InterPro; IPR006070; Sua5-like_dom.
DR InterPro; IPR011125; Znf_HypF.
DR NCBIfam; TIGR00143; hypF; 1.
DR PANTHER; PTHR42959; CARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR42959:SF1; CARBAMOYLTRANSFERASE HYPF; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR Pfam; PF17788; HypF_C; 1.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR Pfam; PF07503; zf-HYPF; 2.
DR PIRSF; PIRSF006256; CMPcnvr_hdrg_mat; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 5..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 202..384
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 732 AA; 84570 MW; 992F11201F09EF27 CRC64;
MSHFGYEIHI KGLVQGVGFR PFVFNIAKEL NLKGEVYNNS LGVVIILECS NDELEIFKEK
LFANLPPLAR IDDFNFSYKK LQKTYNDFSI STSQDSEKFS PILSDFALCE DCYNEFYDEK
NPRFKYPFIT CTNCGPRFSI IKKLPYDRVN TTMDEFKMCS FCQSEYEDPT NRRFHAQPLS
CPKCKITIFL KDKNQNILAK DEKAFILLAK LLEEGQIIAF KGMGGFHLIC DSTNENAINE
LRIRKNRPKK PFAIMVKDLK MAQELAFINE AEAKLLTSNL KPIVILNSKN IHKSLAPDTN
KIGIMLAYMG THLMLFEHFK KPIIATSANL SSQSIIYEET KLLEQLSDVF DFYLDYDRAI
HNSSDDSIAQ VIGKEVMFLR TSRGLNPLYI NTADIFNVKE NILALGSELK NEFACFFKNQ
IFISPYIGDM KSLDIQERFF KILTFFQNSY RLNFDHILSD KHPQFNYVKE FRDYKNFRVQ
HHYAHLCACL FEHKIYKNDV LAFIFDGTGY GDDGKIWGGE IFRANLKSYE RLNHFKNFKL
INADIKNIAN LALALIFDFN LESKASEFLA KFSQVKLNNL KKIHTQSSLY TSSLGRIIDA
FGAFAFDIQK LDYEAQIGLL MEKYYDKNLD YSYKFDIKEK EICFKNAFLQ ALEDKDKVKI
STGLLNGIAD LIIEYSKDFK EEVLLCGGIF QNKTLLEILD QKNFAYKTSL QFPCNDSSIA
LGQLVHYLSL KT
//
